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Glutathione Transferase: New Model for Glutathione Activation
Chemistry – A European Journal, 2008AbstractGlutathione transferases are enzymes of the cellular detoxification system that metabolize a vast spectrum of xenobiotic and endobiotic toxic compounds. They are homodimers or heterodimers and each monomer has an active center composed of a G‐site in which glutathione (GSH) binds and an H‐site for the electrophilic substrate.
Daniel F A R, Dourado +3 more
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Detoxication reactions of glutathione and glutathione transferases
Xenobiotica, 1986(1986). Detoxication reactions of glutathione and glutathione transferases. Xenobiotica: Vol. 16, No. 10-11, pp. 957-973.
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Glutathione transferases: Nomenclature
Biochemical Pharmacology, 1984W B, Jakoby, B, Ketterer, B, Mannervik
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Microsomal Glutathione Transferase 1
2005Microsomal glutathione transferase 1 (MGST1) is an abundant membrane-bound glutathione transferase and peroxidase constituting 3% of the endoplasmic reticulum protein in rat liver (and 5% of the outer mitochondrial membrane). The enzyme is most well studied in mammals and belongs to a large and widely distributed superfamily.
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1995
Glutathione S-transferases (GSTs) are a group of phase II detoxification enzymes of wide tissue distribution. They are classified into three groups, alpha, mu, and pi, on the basis of their chromosomal location, isoelectric point, and immunoreactivity.
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Glutathione S-transferases (GSTs) are a group of phase II detoxification enzymes of wide tissue distribution. They are classified into three groups, alpha, mu, and pi, on the basis of their chromosomal location, isoelectric point, and immunoreactivity.
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Parkinson's disease, pesticides, and glutathione transferase polymorphisms
Lancet, The, 1998Anneke C Blackburn, George D Mellick
exaly